Evidence map›Paper›PMID 32033221›Full record

ArticleBiomolecules2020

Macromolecular Crowding Increases the Affinity of the PHD of ING4 for the Histone H3K4me3 Mark.

Alicia Palacios, Francisco J Blanco

Open access · goldAbstract read
In one paragraph

Article in Biomolecules, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.3field-weighted citation impact, top 44% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

2 citing papers in PubMed, 4 citations in OpenAlex.

  1. Article
  2. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors at 2 institutions in 1 country.

Alicia PalaciosCIC bioGUNE, Bizkaia Science and Technology Park, bld 800, 48160 Derio, Bizkaia, Spain.
Francisco J BlancoCIC bioGUNE, Bizkaia Science and Technology Park, bld 800, 48160 Derio, Bizkaia, Spain.
Euskadiko Parke Teknologikoa · ESIkerbasque · ES

Funding

Ministerio de Ciencia, Innovación y Universidades CTQ2017-83810-R
6 · The paper itself

Abstract

The five members of the family of tumor suppressors ING contain a Plant Homeodomain (PHD) that specifically recognizes histone H3 trimethylated at lysine 4 (H3K4me3) with an affinity in the low micromolar range. Here, we use NMR to show that in the presence of 15% Ficoll 70, an inert macromolecular crowding agent, the mode of binding does not change but the affinity increases by one order of magnitude. The affinity increases also for unmethylated histone H3 tail, but the difference with H3K4me3 is larger in the presence of Ficoll. These results indicate that in the cellular milieu, the affinity of the ING proteins for their chromatin target is larger than previously thought.

Indexed as

Binding SitesCell Cycle ProteinsFicollHistonesHomeodomain ProteinsHumansNuclear Magnetic Resonance, BiomolecularProtein BindingProtein DomainsProtein Interaction MapsTumor Suppressor ProteinsCell Cycle ProteinsFicollhistone H3 trimethyl Lys4HistonesHomeodomain ProteinsING4 protein, humanTumor Suppressor ProteinsH3K4me3histone H3ING4macromolecular crowdingNMRPHDprotein–protein interaction

Identifiers

PMID32033221
PMCPMC7072245
OpenAlexW3004565270

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.